1f80

HOLO-(ACYL CARRIER PROTEIN) SYNTHASE IN COMPLEX WITH HOLO-(ACYL CARRIER PROTEIN)


The B. subtilis AcpS trimer (1f80) binds three molecules of the acyl carrier protein (ASP). The interactions between B. subtilis AcpS and ACP are predominantly electrostatic. The B. subtilis AcpS (white) is shown in spacefill representation, the agrinines, lysines, and histidines are colored blue, while aspartates and glutamates are colored red. The ACP molecule (lime ) is shown in ribbon representation with aspartates and glutamates as sticks and colored red. The B. subtilis AcpS has large electropositive interface with ASP. Electrostatic representation of Mycobacterium tuberculosis (Mtb) AcpS (3hqj) surface using the similar orientation as B. subtilis AcpS, shows a moderate electronegative nature in the putative ACP binding site near the ASP 15. The Mtb ASPM structure (1klp, corresponding to ACP) demonstrates considerably lower negative charge. So, the electrostatic interactions between Mtb AcpS and ASPM are, probably, less important.

About this Structure
1F80 is a 6 chains structure of sequences from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference
Page seeded by OCA on Mon Feb 16 23:04:18 2009